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Blood, Vol. 93 No. 8 (April 15), 1999:
pp. 2454-2462
RAPID COMMUNICATION
A CD4-Independent Interaction of Human Immunodeficiency Virus-1 gp120
With CXCR4 Induces Their Cointernalization, Cell Signaling, and T-Cell
Chemotaxis
Dorothée Missé,
Martine Cerutti,
Nelly Noraz,
Patrick Jourdan,
Jean Favero,
Gérard Devauchelle,
Hans Yssel,
Naomi Taylor, and
Francisco Veas
From the Laboratoire d'Immunologie Rétrovirale et
Moléculaire, Institut de Recherches pour le Développement,
Montpellier, France; the Centre National de la Recherche Scientifique
(CNRS), URA 2209, INRA, Saint Christol lez Alès, France; the
Institut de Génétique Moléculaire, CNRS UMR 5535, Montpellier, France; the Institut National de la Recherche
Médicale (INSERM), U 454, Montpellier, France; and the
Université de Montpellier II, USTL, INSERM U 431, Montpellier,
France.
The gp120 envelope glycoprotein of human immunodeficiency virus-1
(HIV-1) interacts with the CXCR4 chemokine receptor, but it is not
known whether gp120 activates CXCR4-mediated signaling cascades in the
same manner as its natural ligand, SDF1 . We assessed the effects of
wild-type gp120 and a mutant gp120 that interacts with CXCR4 but not
CD4 on CD4 /CXCR4+ cells and
CD4+/CXCR4+ cells, respectively. Under both
experimental conditions, the interaction of CXCR4 and gp120 resulted in
their CD4-independent cointernalization. Both molecules were
translocated into early endosomes, whereas neither protein could be
detected in late endosomes. Binding of gp120 to CXCR4 resulted in a
CD4-independent phosphorylation of Pyk2 and an induction of chemotactic
activity, demonstrating that this interaction has functional
consequences. Interestingly, however, whereas SDF1 activated the
ERK/MAP kinase pathway, this cascade was not induced by gp120.
Together, these results suggest that the pathology of HIV-1 infection
may be modulated by the distinct signal transduction pathway mediated
by gp120 upon its interaction with CXCR4.
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